Calmodulin activation of rat lung adenylate cyclase is independent of the cytoplasmic factors modulating the enzyme.
Adenylate cyclase activity in the rat lung membranes washed with 150 microM-EGTA was stimulated by calmodulin in the presence of 100 microM-Ca2+. The calmodulin activation of the enzyme was concentration-dependent; however, at high concentrations the activation was diminished. Activation of adenylate cyclase by calmodulin was immediate, reversible and due to an increase in the Vmax. without apparent effect on the affinity of the enzyme for ATP. The rat lung supernatant produced additive activation of the adenylate cyclase that was already maximally stimulated by calmodulin, indicating that either calmodulin and cytoplasmic factors act at different sites on adenylate cyclase or different adenylate cyclases may be involved. The data further support our previous conclusion that calmodulin is not involved in the activation of adenylate cyclase by cytoplasmic factors in rat lungs.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D002147:Calmodulin / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002474:Cell-Free System; D003593:Cytoplasm / Q000378:metabolism; D004533:Egtazic Acid / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D008168:Lung / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D004533:Egtazic Acid; D000262:Adenylyl Cyclases